SitesBLAST
Comparing RR42_RS07975 FitnessBrowser__Cup4G11:RR42_RS07975 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 95% coverage: 20:440/444 of query aligns to 143:588/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (≠ ST 155:156) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 176:179) binding
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ I230) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 95% coverage: 20:440/444 of query aligns to 143:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A129), T258 (≠ G132), S281 (= S155), G302 (≠ T176), G303 (= G177), S305 (= S179), S472 (≠ A326), I532 (≠ F386), M539 (≠ L393)
Sites not aligning to the query:
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
37% identity, 81% coverage: 15:374/444 of query aligns to 10:377/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 96% coverage: 19:443/444 of query aligns to 41:490/507 of Q84DC4
- K100 (= K80) mutation to A: Abolishes activity on mandelamide.
- S180 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- S181 (≠ T156) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G177) mutation to A: Increase in KM values for aromatic substrates, but not aliphatic substrates. Active against lactamide but not against mandelamide; when associated with H-207 and E-382.; mutation to V: Increase in KM values for aromatic substrates, but not aliphatic substrates.
- S204 (= S179) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I182) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with E-382. Active against lactamide but not against mandelamide; when associated with A-202 and E-382. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with S-316 and N-437.
- S316 (≠ A298) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- Q382 (≠ A352) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with H-207. Active against lactamide but not against mandelamide; when associated with A-202 and H-207.
- I437 (≠ L393) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with I-31. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-316.
Sites not aligning to the query:
- 31 T→I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
35% identity, 56% coverage: 43:290/444 of query aligns to 42:303/485 of 2f2aA
- active site: K79 (= K80), S154 (= S155), S155 (≠ T156), S173 (≠ T174), T175 (= T176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ I182)
- binding glutamine: G130 (≠ S131), S154 (= S155), D174 (= D175), T175 (= T176), G176 (= G177), S178 (= S179), F206 (≠ L207)
Sites not aligning to the query:
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
35% identity, 56% coverage: 43:290/444 of query aligns to 42:303/485 of 2dqnA
- active site: K79 (= K80), S154 (= S155), S155 (≠ T156), S173 (≠ T174), T175 (= T176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ I182)
- binding asparagine: M129 (≠ F130), G130 (≠ S131), T175 (= T176), G176 (= G177), S178 (= S179)
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
30% identity, 85% coverage: 2:377/444 of query aligns to 1:387/457 of 5h6sC
- active site: K77 (= K80), S152 (= S155), S153 (≠ T156), L173 (≠ T176), G174 (= G177), G175 (= G178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A129), R128 (≠ S131), W129 (≠ G132), S152 (= S155), L173 (≠ T176), G174 (= G177), S176 (= S179), W306 (≠ N296), F338 (≠ R330)
Q9FR37 Amidase 1; AtAMI1; Translocon at the outer membrane of chloroplasts 64-I; AtTOC64-I; EC 3.5.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
46% identity, 34% coverage: 72:222/444 of query aligns to 28:180/425 of Q9FR37
- K36 (= K80) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S155) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (≠ T156) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D175) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S179) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C187) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
33% identity, 94% coverage: 7:422/444 of query aligns to 4:418/461 of 4gysB
- active site: K72 (= K80), S146 (= S155), S147 (≠ T156), T165 (= T174), T167 (= T176), A168 (≠ G177), G169 (= G178), S170 (= S179), V173 (≠ I182)
- binding malonate ion: A120 (= A129), G122 (≠ S131), S146 (= S155), T167 (= T176), A168 (≠ G177), S170 (= S179), S193 (≠ A202), G194 (= G203), V195 (≠ A204), R200 (≠ T209), Y297 (≠ A298), R305 (≠ A306)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
35% identity, 53% coverage: 57:290/444 of query aligns to 49:296/478 of 3h0mA
- active site: K72 (= K80), S147 (= S155), S148 (≠ T156), S166 (≠ T174), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ I182)
- binding glutamine: M122 (≠ F130), G123 (≠ S131), D167 (= D175), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), F199 (≠ L207)
Sites not aligning to the query:
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
35% identity, 53% coverage: 57:290/444 of query aligns to 49:296/478 of 3h0lA
- active site: K72 (= K80), S147 (= S155), S148 (≠ T156), S166 (≠ T174), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ I182)
- binding asparagine: G123 (≠ S131), S147 (= S155), G169 (= G177), G170 (= G178), S171 (= S179)
Sites not aligning to the query:
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
37% identity, 63% coverage: 8:288/444 of query aligns to 8:309/487 of 1m21A
- active site: K81 (= K80), S160 (= S155), S161 (≠ T156), T179 (= T174), T181 (= T176), D182 (≠ G177), G183 (= G178), S184 (= S179), C187 (≠ I182)
- binding : A129 (= A129), N130 (vs. gap), F131 (= F130), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ I182), I212 (≠ L207)
Sites not aligning to the query:
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 97% coverage: 13:442/444 of query aligns to 7:456/468 of 3kfuE
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 83% coverage: 72:440/444 of query aligns to 87:497/508 of 3a1iA
- active site: K95 (= K80), S170 (= S155), S171 (≠ T156), G189 (≠ T174), Q191 (≠ T176), G192 (= G177), G193 (= G178), A194 (≠ S179), I197 (= I182)
- binding benzamide: F145 (= F130), S146 (= S131), G147 (= G132), Q191 (≠ T176), G192 (= G177), G193 (= G178), A194 (≠ S179), W327 (≠ L292)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
36% identity, 52% coverage: 7:239/444 of query aligns to 6:244/564 of 6te4A
Sites not aligning to the query:
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
27% identity, 83% coverage: 70:439/444 of query aligns to 28:449/450 of 4n0iA
- active site: K38 (= K80), S116 (= S155), S117 (≠ T156), T135 (= T174), T137 (= T176), G138 (= G177), G139 (= G178), S140 (= S179), L143 (≠ I182)
- binding glutamine: G89 (≠ S131), T137 (= T176), G138 (= G177), S140 (= S179), Y168 (≠ L207), Y271 (vs. gap), Y272 (vs. gap), R320 (= R328), D404 (≠ R394)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 84% coverage: 52:422/444 of query aligns to 64:441/605 of Q936X2
- K91 (= K80) mutation to A: Loss of activity.
- S165 (= S155) mutation to A: Loss of activity.
- S189 (= S179) mutation to A: Loss of activity.
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
27% identity, 76% coverage: 73:411/444 of query aligns to 62:421/593 of Q9MUK5
Sites not aligning to the query:
- 516 N→A: Loss of HSP90 binding, but no effect on HSP70 binding.
- 550 R→A: 80% decrease of HSP70 and HSP90 binding.
Q9TUI8 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Sus scrofa (Pig) (see paper)
40% identity, 36% coverage: 61:221/444 of query aligns to 127:287/579 of Q9TUI8
- S217 (= S155) mutation to A: Loss of activity.
- S218 (≠ T156) mutation to A: Lowers activity by at least 98%.
- D237 (= D175) mutation D->E,N: Loss of activity.
- S241 (= S179) mutation to A: Loss of activity.
- C249 (= C187) mutation to A: Loss of activity.
2wj1A 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with 7-phenyl-1-(4-(pyridin-2-yl)oxazol-2-yl) heptan- 1-one, an alpha-ketooxazole (see paper)
40% identity, 34% coverage: 72:221/444 of query aligns to 101:254/543 of 2wj1A
- active site: K109 (= K80), S184 (= S155), S185 (≠ T156), T203 (= T174), I205 (≠ T176), G206 (= G177), G207 (= G178), S208 (= S179), F211 (≠ I182)
- binding 7-phenyl-1-(4-pyridin-2-yl-1,3-oxazol-2-yl)heptane-1,1-diol: S157 (≠ F128), M158 (≠ A129), F159 (= F130), S184 (= S155), T203 (= T174), D204 (= D175), I205 (≠ T176), G206 (= G177), S208 (= S179), C236 (≠ A204)
Sites not aligning to the query:
Query Sequence
>RR42_RS07975 FitnessBrowser__Cup4G11:RR42_RS07975
MSTTLPTIAALAADLAAGRTTSVALTEQALARIDGHRNAGGTAFLEVDGAGALAAARAAD
QARAAGLVASPLAGLPVSIKDLFDVKGQVTRAGSKALAGEPASADAPVVARLRAAGAVLI
GRTNMSEFAFSGLGLNPHYGTPRTPFDDARIAGGSTSGGALSVALDLAVAALGTDTGGSI
RIPSAFCGLTGFKPTASRVPLAGAVPLSTSLDSAGPLARSVACCAAFDAIVSGETLDSRP
APLGGLRLLVTRDFVCDGLDAEVAQAFDVTLATLSRLGAQIIPFDFPELKRLPQINAAGG
LTAAEAWHWHKPLLAERGDAYDPRVAMRIRRGEQLGAADYIELLAERRAMQARAAGLLRE
ADAWLMPTVAVRPPRLDALQSDEAFFATNGLVLRNPSVLNFLDGCAVSLPMPAAEQGMGL
SVGGLNGRDARVLQVAGAIEAALR
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory